Adenylate kinase of Escherichia coli: evidence for a functional interaction in phospholipid synthesis.
Adenylate kinase of Escherichia coli: evidence for a functional interaction in phospholipid synthesis.
复制标题
大肠杆菌的腺苷酸激酶：磷脂合成中功能相互作用的证据。
DOI：
10.1021/bi00530a032
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
CronanJr,JE
中科院分区：
文献类型：
--
作者：
Goelz,SE;CronanJr,JE
摘要：以往的遗传学和生物化学实验表明，大肠埃希菌的腺苷酸激酶可能通过与膜结合酶S 1-甘油-3-磷酸酰基转移酶形成复合体直接参与磷脂合成。在这篇文章中，我们报道了检验这一假设的直接实验。描述了腺苷酸激酶结构基因内的突变，该突变导致温度敏感的磷脂合成(在体内检测)和温度敏感的酰基转移酶。无论是在体外还是用三磷酸腺苷测定，该菌株的腺苷酸激酶活性都只有很小的变化。
Susan E. Goelz1*** and John E. Crona* n, Jr.*’5 abstract: Previous genetic and biochemical experiments have suggested that the adenylate kinase of Escherichia coli may be directly involved in phospholipid synthesis through formation of a complex with s «-glycerol-3-phosphate acyltransferase, the membrane-bound enzyme that catalyzes the first step in phospholipid synthesis. In this paper we report direct experiments to test this hypothesis. A mutation within the adenylate kinase structural gene is described that results in a temperature-sensitive phospholipid synthesis (assayed in vivo) and a temperature-sensitive acyltransferase. The ade-nylate kinase activity of this strain is only minimally altered either in vitro or [as assayed by adenosine 5'-triphosphate